JPH03139291A - Method for treating shell of crustacea using enzyme - Google Patents
Method for treating shell of crustacea using enzymeInfo
- Publication number
- JPH03139291A JPH03139291A JP1275330A JP27533089A JPH03139291A JP H03139291 A JPH03139291 A JP H03139291A JP 1275330 A JP1275330 A JP 1275330A JP 27533089 A JP27533089 A JP 27533089A JP H03139291 A JPH03139291 A JP H03139291A
- Authority
- JP
- Japan
- Prior art keywords
- chitin
- calcium carbonate
- protein
- cuticle
- shell
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 238000000034 method Methods 0.000 title claims abstract description 22
- 241000238424 Crustacea Species 0.000 title claims abstract description 9
- 102000004190 Enzymes Human genes 0.000 title description 7
- 108090000790 Enzymes Proteins 0.000 title description 7
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 claims abstract description 42
- 229920002101 Chitin Polymers 0.000 claims abstract description 39
- 229910000019 calcium carbonate Inorganic materials 0.000 claims abstract description 21
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 20
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 20
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims abstract description 12
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims abstract description 10
- 150000001413 amino acids Chemical class 0.000 claims abstract description 10
- 239000011575 calcium Substances 0.000 claims abstract description 10
- 229910052791 calcium Inorganic materials 0.000 claims abstract description 10
- 108091005804 Peptidases Proteins 0.000 claims abstract description 8
- 239000004365 Protease Substances 0.000 claims abstract description 8
- 239000002253 acid Substances 0.000 claims abstract description 7
- 238000010306 acid treatment Methods 0.000 claims abstract description 7
- 241000238557 Decapoda Species 0.000 claims abstract description 6
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 6
- 238000001914 filtration Methods 0.000 claims abstract description 6
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims abstract description 5
- 238000011282 treatment Methods 0.000 claims description 20
- 239000002244 precipitate Substances 0.000 claims description 4
- 241000186361 Actinobacteria <class> Species 0.000 claims description 2
- 238000003672 processing method Methods 0.000 claims 2
- 238000004519 manufacturing process Methods 0.000 abstract description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 abstract description 9
- 239000000126 substance Substances 0.000 abstract description 7
- 239000000203 mixture Substances 0.000 abstract description 5
- 239000007864 aqueous solution Substances 0.000 abstract description 3
- 238000000354 decomposition reaction Methods 0.000 abstract description 2
- 241000186046 Actinomyces Species 0.000 abstract 2
- 229940071106 ethylenediaminetetraacetate Drugs 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 15
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- 229940024606 amino acid Drugs 0.000 description 8
- 235000001014 amino acid Nutrition 0.000 description 8
- 229940088598 enzyme Drugs 0.000 description 6
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000003513 alkali Substances 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 235000009582 asparagine Nutrition 0.000 description 3
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 229960002429 proline Drugs 0.000 description 3
- 230000035484 reaction time Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- BMGWZHWESYHXHC-UHFFFAOYSA-N 2-amino-3-methylpentanoic acid;2-amino-4-methylpentanoic acid Chemical compound CCC(C)C(N)C(O)=O.CC(C)CC(N)C(O)=O BMGWZHWESYHXHC-UHFFFAOYSA-N 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 229920001661 Chitosan Polymers 0.000 description 2
- 235000019750 Crude protein Nutrition 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 239000000853 adhesive Substances 0.000 description 2
- 230000001070 adhesive effect Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 235000019784 crude fat Nutrition 0.000 description 2
- 108010005400 cutinase Proteins 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 235000013930 proline Nutrition 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- VZSRBBMJRBPUNF-UHFFFAOYSA-N 2-(2,3-dihydro-1H-inden-2-ylamino)-N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]pyrimidine-5-carboxamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C(=O)NCCC(N1CC2=C(CC1)NN=N2)=O VZSRBBMJRBPUNF-UHFFFAOYSA-N 0.000 description 1
- YLZOPXRUQYQQID-UHFFFAOYSA-N 3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]propan-1-one Chemical compound N1N=NC=2CN(CCC=21)CCC(=O)N1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F YLZOPXRUQYQQID-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- HSRJKNPTNIJEKV-UHFFFAOYSA-N Guaifenesin Chemical compound COC1=CC=CC=C1OCC(O)CO HSRJKNPTNIJEKV-UHFFFAOYSA-N 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- FXHOOIRPVKKKFG-UHFFFAOYSA-N N,N-Dimethylacetamide Chemical compound CN(C)C(C)=O FXHOOIRPVKKKFG-UHFFFAOYSA-N 0.000 description 1
- 108010059712 Pronase Proteins 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000003905 agrochemical Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 235000019169 all-trans-retinol Nutrition 0.000 description 1
- 238000000149 argon plasma sintering Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000006196 deacetylation Effects 0.000 description 1
- 238000003381 deacetylation reaction Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000002296 dynamic light scattering Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- -1 feed Substances 0.000 description 1
- 239000003337 fertilizer Substances 0.000 description 1
- 239000010419 fine particle Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000012041 food component Nutrition 0.000 description 1
- 239000005417 food ingredient Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
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- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
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Landscapes
- Meat, Egg Or Seafood Products (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Abstract
Description
【発明の詳細な説明】
一上の下１
本発明は酵素を用いる甲殻類の甲殻（クチクラ）の処理
方法に関するもので、特にエビ、カニ等の甲殻類のクチ
クラ（甲殻外骨格）に放線菌由来のプロテアーゼである
アグチナーゼを作用させることによって蛋白質及び炭酸
カルシウムを分離したものを、さらに酸処理してキチン
を単離精製し甲殻の他の主構成成分たる蛋白質をアミノ
酸水溶液、炭酸カルシウムは天然のままの炭酸カルシウ
ムの沈殿として取得することでクチクラ申のすべての有
効成分を利用するためのクチクラの処理方法に関するも
のである。DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for treating crustacean shells (cuticles) using enzymes. Proteins and calcium carbonate are separated by the action of agtinase, a protease derived from the plant, and then acid-treated to isolate and purify chitin. The present invention relates to a method for processing cuticle in order to utilize all the active ingredients of the cuticle by obtaining it as a precipitate of intact calcium carbonate.
従」Ｌの」［夜
地球上にあって最も豊富かつ利用されているバイオマス
資源であるセルロースの自然界における生産量は、年間
１０００億トンともいわれるが。The natural production of cellulose, the most abundant and used biomass resource on earth, is said to be 100 billion tons per year.
キチンの年間生産量もまた１００億、あるいはセルロー
スに匹敵する１０００億トンともいわれている。キチン
は今までのところ、その脱アセチル生成物であるキトサ
ンに変換され凝集剤として水処理に利用されているほか
、近年になってキチンキトサンの持つ化学的あるいは生
物学的な特性機能が解明され、それに基づき食品、化粧
品、医薬、農薬等の分野において活発な利用研究が行わ
れ、特徴ある新製品が生み出されている。キチンはＮ−
７セチルーＤ−グルコサミン残基が多数β−（ｌ、０結
合した多糖で、甲殻類並びに昆虫類の外皮骨格組成、菌
類の細胞壁の構成成分としてよく知られている。 エビ
、カニ等の甲殻類のクチクラは炭酸カルシウム、蛋白質
、キチンを主成分として構成され、一般にこの甲殻（ク
チクラ）の化学的処理によりキチンの工業的製造が行わ
れておりまた、実験的には微生物、酵素を用いた生物化
学的処理によるキチンの製造も検討されている。The annual production of chitin is also said to be 10 billion tons, or 100 billion tons, which is comparable to cellulose. Until now, chitin has been converted to its deacetylated product, chitosan, and used as a flocculant in water treatment, and in recent years, the chemical and biological properties and functions of chitin and chitosan have been elucidated. Based on this, active research on its use in the fields of food, cosmetics, medicine, agrochemicals, etc. is being conducted, and unique new products are being created. Chitin is N-
It is a polysaccharide in which many 7cetyl-D-glucosamine residues are linked with β-(l,0), and it is well known as a component of the exoskeleton of crustaceans and insects, and of the cell wall of fungi. Crustaceans such as shrimp and crabs The cuticle of the human body is mainly composed of calcium carbonate, protein, and chitin, and chitin is generally produced industrially by chemically processing this carapace (cuticle). Production of chitin through chemical treatment is also being considered.
キチンの製造工程自体はそう複雑なものではないが、化
学処理法は製造工程で、酸処理とアルカリ処理を必要と
するため、洗浄等に大量の水を必要とし廃水の処理に多
額の費用がかかるほか、また、酸処理工程の温度が分子
量に影響する等、アルカリや酸の濃度、反応時間、反応
温度等の反応条件の違いによって、得られる製品の純度
や品質が異なってくるばかりでなく、更に熱アルカリや
酸によるグリコシド結合の加水分解による分子量低下を
避は得ない欠点がある。Although the chitin production process itself is not very complicated, the chemical treatment method requires acid treatment and alkali treatment during the manufacturing process, which requires a large amount of water for cleaning etc., and wastewater treatment costs a lot of money. In addition to this, the temperature of the acid treatment process affects the molecular weight, and differences in reaction conditions such as concentration of alkali and acid, reaction time, and reaction temperature not only cause differences in the purity and quality of the resulting product. Furthermore, there is a disadvantage that molecular weight inevitably decreases due to hydrolysis of glycosidic bonds by hot alkalis or acids.
これらの化学処理法の欠点を解決すべく、微生物や酵素
を用いた生物化学的処理方法が研究されるようになり、
キチン製造における除蛋白工程にプロテアーゼを用いる
ことが試みられ、プロナーゼ、パパイン５ペプシンなど
種々のプロテアーゼを用いた実験が行われているほか、
最近ではプロテアーゼ生産菌を用いることも試みられて
いる。In order to solve the drawbacks of these chemical treatment methods, research began on biochemical treatment methods using microorganisms and enzymes.
Attempts have been made to use proteases in the protein removal process in chitin production, and experiments have been conducted using various proteases such as pronase and papain-5-pepsin.
Recently, attempts have also been made to use protease producing bacteria.
これら生物化学的処理方法は従来のアルカリ処理法と比
較して脱アセチル、解重合などの副反応を起こさないた
め、変性の少ない比較的高分子量のキチンが得られるほ
か、処理温度が低いなどの利点があるものの、−貫した
生物化学処理による蛋白質の完全除去はいまだ達成され
てなく、あくまでも酸処理による除カルシウム工程を前
提にしたものであって、しかもキチン以外の甲殻（クチ
クラ）の主構成成分たる蛋白質や炭酸カルシウムの利用
に関しては何等の関心が持たれていない実態にある。Compared to conventional alkali treatment methods, these biochemical treatment methods do not cause side reactions such as deacetylation and depolymerization, so chitin with a relatively high molecular weight and less denaturation can be obtained, and the processing temperature is low. Although there are advantages, complete removal of proteins by comprehensive biochemical treatment has not yet been achieved, and this method is based on the premise of a calcium removal process by acid treatment, and furthermore, the main constituent of the carapace (cuticle) other than chitin The reality is that there is no interest in the utilization of the protein and calcium carbonate components.
が しようと る 占
従って本発明は生物化学的処理による高分子量キチン製
造に際し、化学処理工程を出来るだけ少なくするための
ものであり、特に化学処理工程における酸処理工程を不
要にする生物化学的処理によるキチンの製造法を提供す
るためのものであって、その際の蛋白質の完全除去と副
生成分の有効利用を計るためのものである
占 るための
すなわち、本発明はエビ、カニ等の甲殻類の甲殻（クチ
クラ）に放線菌由来のプロテアーゼであるアクチナーゼ
を作用させることによって蛋白質及びカルシウムを除去
分離した後、キチン中の残存カルシウムを酸処理により
除去することを特徴とする甲殻類の甲殻（クチクラ）の
処理方法に関するもので、本発明の方法では先ず、甲殻
を数平方センチメーターの大きさのチップに切断するが
細かすぎると以下に述べる炭酸カルシウムとの分離が難
しくなる。勿論、酵素の作用に関しては如何に細かくし
ても不都合ということはない０次に、ｐＨ５〜７に調整
した水に、切断した甲殻と７クチナーゼを加える。この
場合最適ｐＨは６である。アクチナーゼのカゼインに対
する最適ＰＨは科研製薬（株）の試料では７．０〜９．
０であるが１本発明の最適ＰＨが６であるのは甲殻に含
まれる炭酸カルシウムによる影響が考えられる。Accordingly, the present invention is intended to reduce the number of chemical treatment steps as much as possible when producing high molecular weight chitin through biochemical treatment, and in particular, to reduce the number of chemical treatment steps as much as possible in the production of high molecular weight chitin through biochemical treatment. The purpose of the present invention is to provide a method for producing chitin using chitin, which completely removes proteins and makes effective use of by-products. A crustacean shell, characterized in that protein and calcium are removed and separated by acting on the cuticle of the crustacean with actinase, which is a protease derived from actinomycetes, and residual calcium in chitin is removed by acid treatment. In the method of the present invention, the carapace is first cut into chips several square centimeters in size, but if the chips are too small, it will be difficult to separate them from the calcium carbonate described below. Of course, there is no problem in terms of the action of the enzyme, no matter how finely divided it is.Next, the cut carapace and cutinase are added to water whose pH has been adjusted to 5 to 7. In this case the optimum pH is 6. The optimum pH of actinase for casein is 7.0 to 9.0 for samples from Kaken Pharmaceutical Co., Ltd.
0, but the optimum pH of the present invention is 6, which is considered to be due to the influence of calcium carbonate contained in the shell.
アクチナーゼはカルシウムイｊンにより安定化すること
が知られ、特に耐熱性が増加することが示されている、
これらのことがら炭敢カルシウムを含む甲殻試料の蛋白
質分解にはアクチナーゼが極めて適しているものと考え
られる０次に試料を加えた液を３０〜６０°Ｃで攪はん
するが最適温度は５０’Ｏであり、それから離れるにつ
れ蛋白分解速度は小さくなる０反応時間は夫々の条件に
おいて適宜定めるが蛋白質の分解につれ、炭酸カルシウ
ムが沈殿となってかなり除去される。これはキチンと共
に甲殻マトリクスを形成している蛋白質がいわば接着剤
的役割を果たして炭酸カルシウムをそのマトリクスの構
成成分としていたのが、蛋白質という接着剤の分解に伴
ない炭酸カルシウムが離脱するものと思われる。この炭
酸カルシウムは非常に微細な粒子であるがろ過により蛋
白質が分解して生成したアミノ酸水溶液からキチンと共
に分離される。この炭酸カルシウムとキチンは粒度の違
いによりろ過等の通常の物理的手段で容易に分離される
。ここで分離されたキチンにはまだ一部の炭酸力ルシウ
ムンが付着しているが、塩酸またはＥＤＴＡで処理する
ことで炭酸カルシウムを完全に除去したキチンを得るこ
とができる。Actinase is known to be stabilized by calcium ion, and in particular has been shown to increase heat resistance.
Based on these facts, actinase is considered to be extremely suitable for proteolyzing shell samples containing calcium carbonate.The solution to which the sample was added is stirred at 30-60°C, but the optimum temperature is 50°C. The 0 reaction time, in which the proteolytic rate decreases with increasing distance from the 0 reaction time, is determined appropriately for each condition, but as the protein decomposes, a considerable amount of calcium carbonate is removed as a precipitate. This is because the protein that forms the shell matrix together with chitin plays a so-called adhesive role, and calcium carbonate is a component of the matrix, but as the protein adhesive decomposes, the calcium carbonate is released. It will be done. This calcium carbonate is a very fine particle, but it is separated along with chitin from the amino acid aqueous solution produced by protein decomposition through filtration. Due to the difference in particle size, calcium carbonate and chitin can be easily separated by ordinary physical means such as filtration. Although some lucium carbonate still adheres to the chitin separated here, chitin from which calcium carbonate has been completely removed can be obtained by treatment with hydrochloric acid or EDTA.
わＩ
以下に本発明の実施例を示すが、これは本発明の一例を
示すのみであって、これらの実施例により本発明が何等
限定されるものではないことは当然である。Examples of the present invention are shown below, but these are only examples of the present invention, and it goes without saying that the present invention is not limited to these Examples in any way.
実施例１
１）試料
エピ：ノルウェー産（肉部分を除いた甲殻全体）
水分 １０月
灰分 ２０．６
粗脂肪 １１．Ｏ
粗蛋白質 ２３．９
炭水化物 ３４．４
２）操作
０．１Ｍクエン酸緩衝液５００ｍ１に７クチナーゼＥ（
高純度品）２００万チロシン単位と１０１１２程度に切
断したエビ試料２０ｇを加え、５０℃で６０時間反応を
行い蛋白質の分解を行った。Example 1 1) Sample epi: Norwegian (whole shell excluding meat) Moisture October Ash 20.6 Crude fat 11. O Crude protein 23.9 Carbohydrate 34.4 2) Procedure Add 7 cutinase E (
Highly purified product) 2 million tyrosine units and 20 g of a shrimp sample cut into approximately 10112 pieces were added and reacted at 50°C for 60 hours to decompose the protein.
キチンと炭酸カルシウムはろ過によりアミノ酸水溶液か
ら分離した。また、キチンと炭酸カルシウムは粒度の差
によって分けた。ここで得たキチンを２Ｎ塩酸中４８時
間浸漬し無機塩を除去後、蒸留水、エタノール洗浄、乾
燥して精製キチンを得た。Chitin and calcium carbonate were separated from the amino acid aqueous solution by filtration. Furthermore, chitin and calcium carbonate were separated based on the difference in particle size. The chitin obtained here was immersed in 2N hydrochloric acid for 48 hours to remove inorganic salts, washed with distilled water and ethanol, and dried to obtain purified chitin.
３）結果
ａ）アミノ酸：得られたアミノ酸組成を表１、表２（１
が一回目の酵素処理、２が二回目）に示し、表３には資
料の蛋白質を塩酸で加水分解したときのアミノ酸組成を
示した。3) Results a) Amino acids: The obtained amino acid compositions are shown in Table 1 and Table 2 (1
Table 3 shows the amino acid composition when the protein of the sample was hydrolyzed with hydrochloric acid.
ｂ）灰分：収量 ２゜８８ｇ
分析の結果から、カルシウムの割合が多く、灰分のほと
んどが炭酸カルシウムであることが判明した。b) Ash content: Yield 2°88g The analysis results revealed that the proportion of calcium was high and most of the ash content was calcium carbonate.
Ｃ）キチン：収量 １．４３ｇ
蛋白質含量 ０，２８％
除去率 ９９．２ ％
カルシウム含量 ０．０３％
除去率 ９９．７ ％
表 ｌ
Ａｍ１ｎｏ ａｃｉｄ
Ａｓｐａｒａｇｉｎｅ
Ｔｈｒｅｏｎｌｏｎ
ｅｔ１ｎ
Ｇｌｕｔａｍｉｎ＠
Ｐｒｏｌｉｎｅ
Ｇｌｌｃｔｎｅ
Ａｌａｎｉｎｅ
Ｃ！５ｔｉｎｓ
Ｖａ Ｉ ｉｎ＠
Ｍｅｔｈｉｏｎｉｎｓ
Ｉｓｏｌｅｕｃｉｎｅ
Ｌｅｕｃｉｎｅ
Ｔｙｒｏｓｉｎｅ
Ｐｈｅｓｙｌａｌａｎｉｎｅ
ｙｇｉｎｅ
Ｈｉｓｔｉｄｉｎｅ
Ｔｒｙｐｔｏｐｈａｎ
Ａｒｇｉｎｉｎｅ
ル ｇ／ｇ
３３．８１
１６．０Ｂ
１４．１２
３７．８０
１１．４０
２１）、 １４
２２、Ｑ５
２．０４
１？、５Ｑ
８．３Ｂ
１４．８５
２Ｑ、８Ｑ
ｔｓ、ｏｓ
１５、Ｑ２
２０、？Ｑ
６、Ｂ５
１５．０７
表 ２
表 ３
Ａｍｉｎｏ ａｃｉｄ
Ａｓｐａｒａｇｉｎｅ
Ｔｈｒｅｏｒ＋＋ｏｎ
ｅｔ １ｎ
ＧｌｕｔａＩＩＩｉｎｅ
Ｐｒｏｌｉｎｅ
Ｇｌｙｃ＋ｎｅ
Ａｌａｎ＋ｎｅ
ＣｙｓＬｉｎｅ
ａｌｉｎｅ
Ｍｅｔｈｉｏｎｉｎｅ
Ｉｓｏｌｅｕｃｉｎｅ
Ｌｅｕｃｉｎｅ
Ｔｙｒｏｓｉｎｅ
Ｐｈｅｎｙｌａｌａｎｉｎｅ
Ｌヲｓ ｉｎｅ
Ｈｉｓｔｉｄｉｎｅ
Ｔｒｙｐｔｏｐｈａｎ
Ａｒｇｉｎｉｎｅ
弘 ｇ／ｇ
８．７４
８．５０
４．７９
６．３０
２．９２
５．７２
５．５６
０．５８
４．７５
０．４９
２．８７
４．１０
６．３８
３．０８
４．４８
１．９５
３．５３
Ａｍｉｎｏ ａｃｉｄ
Ａｓｐａｒａｇｉｎｅ
Ｔｈｒｅｏｎｉｏｎ
ｅｔｉｎ
ＧｌｕｔａＩＩＩｉｎｅ
Ｐｒｏｌｉｎｅ
ＧｌｙＣｉｎｅ
Ａｌａｎｉｎｓ
Ｃｙｓｔｉｎｅ
ａｌｉｎｓ
Ｍｅｔｈｉｏｎｉｎｅ
Ｉｓｏｌｅｕｃｉｎｅ
Ｌｅｕｃｉｎｅ
Ｔ７ｒｏｓｉｎｅ
Ｐｈｅｎ７１ａｌａｎｉｎｅ
Ｌツｓ ｉｎｅ
Ｈｉｓｔｉｄｉｎｅ
Ｔｒ７ｐｔａｐｈａｎ
Ａｒｇｉｎｉｎｓ
弘 ｇ／ｇ
２４．３２
１０．９７
１５．９４
２Ｂ、８０
１２．１８
１！１１．４１
１４．４７
１４．８３
３．４２
７．５２
１２．０Ｂ
１０３．８１
２Ｂ、５２
８．６２
６．４６
１８．３２
実施例２
１）試料：北海道産毛かに、煮沸処理甲殻水分
６．４１ ％
灰分 ４０−００
粗脂肪 ３．７６
粗蛋白質 ３７．１３
糖質 １２．７０
２）操作
酵素反応終了後の脱灰分操作以外は実施例１と同様の操
作を行った。脱灰分は０．１Ｍ ＥＤＴＡ溶液（ｐＨ
７）中で２４時間１回、４８時間１回浸漬攪はんして行
った。C) Chitin: Yield 1.43g Protein content 0.28% Removal rate 99.2% Calcium content 0.03% Removal rate 99.7% Table l Am1no acid Asparagine Threonlon et1n Glutamin @ Proline Gllctn e Alanine C! 5tins Va I in@ Methionins Isoleucine Leucine Tyrosine Phesylanine Ygine Histidine Tryptophan Arginine Le g/g 33.81 16.0 B 14.12 37.80 11.40 21), 14 22, Q5 2.04 1? , 5Q 8.3B 14.85 2Q, 8Q ts, os 15, Q2 20,? Q 6, B5 15.07 Table 2 Table 3 Amino acid Asparagine Threor++on et 1n GlutaIIIine Proline Glyc+ne Alan+ne CysLine aline Methionine Is Oleucine Leucine Tyrosine Phenylanine Lwasine Histidine Tryptophan Arginine Hiroshi g/g 8.74 8.50 4.79 6. 30 2.92 5.72 5.56 0.58 4.75 0.49 2.87 4.10 6.38 3.08 4.48 1.95 3.53 Amino acid Asparagine Threonion etin GlutaIIIine Prol ine GlyCine Alanins Cystine alins Methionine Isoleucine Leucine T7rosine Phen71alanine Ltsusine Histidine Tr7ptaphan Arginins Hiroshi g/g 24.32 10.97 15.9 4 2B, 80 12.18 1!11.41 14.47 14.83 3.42 7.52 12 .0B 103.81 2B, 52 8.62 6.46 18.32 Example 2 1) Sample: Hokkaido downy crab, boiled shell water
6.41% Ash 40-00 Crude fat 3.76 Crude protein 37.13 Carbohydrate 12.70 2) Operation The same operation as in Example 1 was performed except for the deashing operation after the enzyme reaction was completed. The deashing content was determined using a 0.1M EDTA solution (pH
7) by immersion stirring once for 24 hours and once for 48 hours.
３）結果
キチン：
収量 ２．１ｇ
蛋白質含量
除去率
カルシウム含量
除去率
絶対分子量 １３
０ 、３８ ％
９８．８ ％
ｔ ｒａｃｅ
１００．０ ％
、０７Ｘ１０５
なお、絶対分子量はキチンを塩化リチウムを含むジメチ
ルアセトアミドに溶解し、静的光散乱を利用した光散乱
光度計（大域電子（株）類ダイナミック光散乱光度計Ｄ
Ｓ Ｌ−７００）を用いて測定した。3) Results Chitin: Yield 2.1g Protein content removal rate Calcium content removal rate Absolute molecular weight 130, 38% 98.8% Trace 100.0%, 07X105 The absolute molecular weight is determined by converting chitin to dimethylacetamide containing lithium chloride. A light scattering photometer that uses dissolved and static light scattering (Daikyu Denshi Co., Ltd. class dynamic light scattering photometer D)
SL-700).
比較例
１）試料 実施例２に同じ
２）操作
試料（冷凍乾燥後粉砕したもの）４４ｇに２Ｎ塩＃ ４
００ ｍ ｌを加え、５時間室温に放置して灰分を除去
した。ろ過により甲殻を回収し、更に２Ｎ塩酸１００ｍ
１にて４８時間、室温で連続攪はんし脱灰を行った。脱
灰終了後、水洗し沸騰水浴中で１２時間、ＩＮ水酸化ナ
トリウムＬｏｏｍｌにて２回除蛋白を行った。後、水洗
、さらにエタノールにて２４時間室温で攪はんし残存す
る色素を除去、エタノールで洗浄後、減圧乾燥してキチ
ンを単離精製した。Comparative Example 1) Sample Same as Example 2 2) Operation Sample (freeze-dried and pulverized) 44g and 2N salt #4
00 ml was added thereto and left at room temperature for 5 hours to remove ash. Collect the shell by filtration and add 100ml of 2N hydrochloric acid.
1 for 48 hours at room temperature for continuous stirring and deashing. After the decalcification was completed, it was washed with water and deproteinized twice in IN sodium hydroxide Looml for 12 hours in a boiling water bath. Thereafter, the mixture was washed with water, and further stirred with ethanol at room temperature for 24 hours to remove the remaining pigment. After washing with ethanol, the mixture was dried under reduced pressure to isolate and purify chitin.
３）結果
絶対分子量 ９．７０Ｘ１０５分析方法は実
施例２と同じ
の量を少なくできるため経済的であるばかりでなく、酸
による変性をも少なくすることができる。3) Result: Absolute molecular weight: 9.70×105 The analysis method is not only economical because it allows the same amount as in Example 2 to be reduced, but also reduces denaturation by acid.
萌」Ｌり」Ｌ釆
本発明によれば、従来の酵素処理法で達成し得なかった
ほぼ完全な蛋白質の除去が達成できるばかりでなく得ら
れるキチンも従来得られなかった高分子量のものとなり
、また、原料の甲殻（クチクラ）を微粉末に粉砕する必
要がなく１このことは酵素処理の過程で沈殿する炭酸カ
ルシウムとキチンの分離を容易にする点で生産上非常に
重要な利点となるもので、今までの酵素処理では考えら
れなかったことである。また１本発明によれば、甲殻（
クチクラ）中の蛋白質はアミノ酸水溶液として回収され
肥料、飼料、食品原料等として。According to the present invention, not only can almost complete protein removal, which could not be achieved with conventional enzyme treatment methods, be achieved, but also the obtained chitin has a high molecular weight, which could not be obtained conventionally. In addition, there is no need to grind the raw material, the cuticle, into a fine powder.1 This is a very important advantage in production, as it facilitates the separation of calcium carbonate and chitin that precipitate during the enzyme treatment process. This is something that would have been unimaginable with conventional enzyme treatments. According to one aspect of the present invention, the shell (
The protein in the cuticle is recovered as an aqueous amino acid solution and used as fertilizer, feed, food ingredients, etc.
Claims (1)
菌由来のプロテアーゼであるアクチナーゼを作用させる
ことによって蛋白質及びカルシウムを除去分離した後、
キチン中の残存カルシウムを酸処理により除去すること
を特徴とする甲殻類の甲殻（クチクラ）の処理方法。 （２）アクチナーゼをｐＨ５〜７で作用させる特許請求
の範囲第１項記載の処理方法。 （３）処理温度が３０〜６０℃である特許請求の範囲第
１項乃至第２項記載の処理方法。（４）甲殻（クチクラ
）中の蛋白質をアミノ酸液として分離回収する特許請求
の範囲第１項乃至第３項記載の処理方法。 （５）甲殻（クチクラ）中の炭酸カルシウムをろ過等物
理的手段で沈殿として分離回収する特許請求の範囲第１
項乃至第３項記載の処理方法。 （６）酸処理が塩酸またはエチレンジアミンテトラ四酢
酸（以下、ＥＤＴＡ）によるものである特許請求の範囲
第１項乃至第３項記載の処理方法。[Claims] (1) After removing and separating proteins and calcium by applying actinase, a protease derived from actinomycetes, to the cuticle of crustaceans such as shrimp and crabs,
A method for treating crustacean shells (cuticles), which comprises removing residual calcium in chitin by acid treatment. (2) The treatment method according to claim 1, in which actinase acts at a pH of 5 to 7. (3) The processing method according to claims 1 and 2, wherein the processing temperature is 30 to 60°C. (4) A treatment method according to claims 1 to 3, in which proteins in the cuticle are separated and recovered as an amino acid solution. (5) Claim 1, in which calcium carbonate in the cuticle is separated and recovered as a precipitate by physical means such as filtration.
The processing method described in items 3 to 3. (6) The treatment method according to any one of claims 1 to 3, wherein the acid treatment is performed using hydrochloric acid or ethylenediaminetetratetraacetic acid (hereinafter referred to as EDTA).
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1275330A JP2870871B2 (en) | 1989-10-23 | 1989-10-23 | A method for treating crustacean shells using enzymes |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1275330A JP2870871B2 (en) | 1989-10-23 | 1989-10-23 | A method for treating crustacean shells using enzymes |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH03139291A true JPH03139291A (en) | 1991-06-13 |
| JP2870871B2 JP2870871B2 (en) | 1999-03-17 |
Family
ID=17553960
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP1275330A Expired - Fee Related JP2870871B2 (en) | 1989-10-23 | 1989-10-23 | A method for treating crustacean shells using enzymes |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2870871B2 (en) |
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| CN103535781A (en) * | 2013-10-23 | 2014-01-29 | 宁波大学 | Method for preparing instant shrimp leisure food |
| JP2018502203A (en) * | 2014-12-31 | 2018-01-25 | インセクト | Enzymatic hydrolysis of chitin, hydrolysates, and insects to produce one or more desired products |
| US11891459B2 (en) | 2014-12-31 | 2024-02-06 | Ynsect | Chitin, hydrolysate and method for the production of one or more desired products from insects by means of enzymatic hydrolysis |
| GB2612617A (en) * | 2021-11-05 | 2023-05-10 | Marine Bioenergy As | Demineralisation of organic tissue |
| WO2023079104A1 (en) * | 2021-11-05 | 2023-05-11 | Marine Bioenergy As | Demineralisation of organic tissue |
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| JP2870871B2 (en) | 1999-03-17 |
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